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6SPW

Structure of protein kinase CK2 catalytic subunit with the CK2beta-competitive bisubstrate inhibitor ARC3140

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005956cellular_componentprotein kinase CK2 complex
A0006302biological_processdouble-strand break repair
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0006974biological_processDNA damage response
A0007165biological_processsignal transduction
A0008284biological_processpositive regulation of cell population proliferation
A0016055biological_processWnt signaling pathway
A0016301molecular_functionkinase activity
A0016605cellular_componentPML body
A0017148biological_processnegative regulation of translation
A0018105biological_processpeptidyl-serine phosphorylation
A0018107biological_processpeptidyl-threonine phosphorylation
A0030177biological_processpositive regulation of Wnt signaling pathway
A0030307biological_processpositive regulation of cell growth
A0031519cellular_componentPcG protein complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0042802molecular_functionidentical protein binding
A0043154biological_processnegative regulation of cysteine-type endopeptidase activity involved in apoptotic process
A0045732biological_processpositive regulation of protein catabolic process
A0048511biological_processrhythmic process
A0050821biological_processprotein stabilization
A0051726biological_processregulation of cell cycle
A0051879molecular_functionHsp90 protein binding
A0061077biological_processchaperone-mediated protein folding
A0070822cellular_componentSin3-type complex
A0075342biological_processsymbiont-mediated disruption of host cell PML body
A0106310molecular_functionprotein serine kinase activity
A1905337biological_processpositive regulation of aggrephagy
A1905818biological_processregulation of chromosome separation
A2000042biological_processnegative regulation of double-strand break repair via homologous recombination
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 401
ChainResidue
ATRP33
ATHR326
AHOH654
AHOH662
AHOH674
AHOH709

site_idAC2
Number of Residues12
Detailsbinding site for residue A0Z B 101
ChainResidue
APHE113
AGLU114
AVAL116
ALYS158
AASP175
AHOH737
AHOH769
BDAS2
BHOH201
AARG47
AGLY48
AVAL53

site_idAC3
Number of Residues5
Detailsbinding site for Di-peptide DAS C 2 and ASP C 3
ChainResidue
AHOH572
CASP4
CA0Z101
CHOH201
DA0Z101

site_idAC4
Number of Residues14
Detailsbinding site for Di-peptide A0Z C 101 and DAS C 2
ChainResidue
ATYR39
ALEU41
ALYS44
AVAL101
ATHR108
AHIS236
AARG244
AHOH572
AHOH575
AHOH725
AHOH780
CASP3
CHOH201
DA0Z101

site_idAC5
Number of Residues5
Detailsbinding site for Di-peptide DAS D 2 and ASP D 3
ChainResidue
AASP266
APRO267
AARG268
DASP4
DA0Z101

site_idAC6
Number of Residues14
Detailsbinding site for Di-peptide A0Z D 101 and DAS D 2
ChainResidue
ALEU41
AVAL42
AASP237
ATYR239
AASP240
AASP266
APRO267
AARG268
AILE272
CDAS2
CA0Z101
CHOH203
DASP3
DHOH202

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VVVK
ChainResidueDetails
ALEU45-LYS68

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
AILE152-ILE164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP156

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS68
ALEU45

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CDK1 => ECO:0000269|PubMed:7592773
ChainResidueDetails
ATHR360
ATHR344

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:7592773
ChainResidueDetails
ASER362

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:7592773, ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER370

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PDB entries from 2024-06-12

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